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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/96106
Crystallization and diffraction of single-crystals at ALBA Synchrotron to structure determination of a Relaxase protein
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The aim of the present work is the structure description of two variant (full length and Nterminal)
of a protein with Relaxase activity. Both pure variants were crystallized using sitting
drop vapor diffusion technique. Crystals obtained were optimized increasing its quality and
some of them were treated to derivatize it with metals.
Diffraction of crystals and pre-treatment of protein were integrally performed in ALBA
Synchrotron (Barcelona) installations. In BL-13 XALOC beamline were collected the data which
were processed and evaluated as good quality data. The phase problem solution was not
possible by applying Molecular Replacement nor detecting the anomalous signal of derivatives
crystals. The lack of phases did not permit to solve the electron density equation, and therefore,
it was not possible to complete the model building
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Treballs Finals de Grau de Química, Facultat de Química, Universitat de Barcelona, Any: 2016, Tutor: Daniel Sainz García i Roeland Boer
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GUEVARA PUIG, Tibisay. Crystallization and diffraction of single-crystals at ALBA Synchrotron to structure determination of a Relaxase protein. [consulted: 11 of October of 2026]. Available at: https://hdl.handle.net/2445/96106